Bioaffinity methods and relevant principles are being developed which can be used for characterizing functional interaction properties, including multi-molecular assembly, of biological macromolecules and for isolating and purifying macromolecules based on these properties. A major current study has been designed to evaluate the potential to adapt bioaffinity chromatography to extant high performance liquid chromatography technology. Silica-based and glass-bead matrices have been evaluated for use to measure protein-protein, peptide-protein, and peptide-peptide interactions, for neuroendocrine peptides and proteins and their precursors as well as well-understood "model" proteins. Analytical high performance affinity chromatographic methods which have resulted from this study provide potentially important analytical biochemistry tools both for characterizing basic properties of these macromolecules and for molecular diagnosis. Also, some high performance affinity methods that have been quantitatively evaluated are suitable for microscale and potentially large-scale isolation of biologically active peptides and proteins.